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Database: UniProt
Entry: A0A091DWG6_FUKDA
LinkDB: A0A091DWG6_FUKDA
Original site: A0A091DWG6_FUKDA 
ID   A0A091DWG6_FUKDA        Unreviewed;      1623 AA.
AC   A0A091DWG6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Alpha-protein kinase 3 {ECO:0000313|EMBL:KFO34630.1};
GN   ORFNames=H920_03998 {ECO:0000313|EMBL:KFO34630.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO34630.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO34630.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO34630.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC       protein kinase family. ALPK subfamily. {ECO:0000256|ARBA:ARBA00008651}.
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DR   EMBL; KN121930; KFO34630.1; -; Genomic_DNA.
DR   RefSeq; XP_010619418.1; XM_010621116.2.
DR   STRING; 885580.ENSFDAP00000009972; -.
DR   GeneID; 104860096; -.
DR   CTD; 57538; -.
DR   eggNOG; ENOG502QPP5; Eukaryota.
DR   OrthoDB; 5321836at2759; -.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 3.20.200.10; MHCK/EF2 kinase; 1.
DR   InterPro; IPR004166; a-kinase_dom.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   PANTHER; PTHR47091; ALPHA-PROTEIN KINASE 2-RELATED; 1.
DR   PANTHER; PTHR47091:SF1; ALPHA-PROTEIN KINASE 3; 1.
DR   Pfam; PF02816; Alpha_kinase; 1.
DR   Pfam; PF07679; I-set; 1.
DR   SMART; SM00811; Alpha_kinase; 1.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51158; ALPHA_KINASE; 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   3: Inferred from homology;
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFO34630.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          60..156
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1194..1282
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1310..1545
FT                   /note="Alpha-type protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS51158"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          824..873
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1034..1074
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1097..1187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1548..1623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..240
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..332
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..371
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..516
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..576
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        580..601
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..672
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        673..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..729
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        775..792
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1097..1113
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1134..1152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1564..1600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1623 AA;  173388 MW;  0B8F15E5FEDB9C9B CRC64;
     MGSRRVPGWG IGGRSGGDSE DDGPVWTPSP ASRSYLLSVR PETRSTFCSI IAQLTEETQP
     LFETTLKSRA VSEDSDVRFT CIVTGYPEPE VTWYKDDTEL DRYCGLPKYK ITHQGNRHTL
     QLYRCQEEDA AIYQASARNT KGIVSCSGVL EVGTMTEYKI HQRWFAKLKR KAAAKMRELE
     QSWRQGKEFP GEAEVLRKLS PDRFQRKRRL SGPGVPIPSA PCPPREAKDE APEVWQEGKT
     ESVRHPGLGL VNNFAAGGEA PTNGEPAPEN GEDREHGLLT YICEAMELEP SKAPQKESGA
     KKKRKDRESK LGLRTLVSEK TARGHKSAEN CVSSSDKADS GGTQRPVGTE QVQAQCRSRA
     AWGSGSSRTD TIRKPAPAVD TQDKAHDGPA QSPVEAPDTS PAPGPGQEGF FSLKDLYVES
     TLEARPQGQG EPLPPSAEGP PGKVLIGSRG AEMSTDPGQH TPSVAPHSAR PFNRKRFAPP
     KPKGEPHTDS QPASSLKGAP DCEVQNSRQA LPQASAQVPT PPARWKHSSR DSPVQGRAGH
     RPSGEEPQAT TAQTMSASNS SSAAPTGHSS SGNQRVVEPM DIKAQEDRRT HTDDRRTRGR
     KSPQVQVVGR TEGERAQAAQ RTQVDVVMQE SESPQSDRSS QKDVVMQRRV ETQVERILAD
     ERTQENRRMQ EGEQTQPEGS VLPATESHPE QQSVTSLSPL PRAPESLPSE GPRSSELTEC
     PTQTPEASSV PEEPGFVLTS EEPPVNTSGS HEDTVLGPLP ASFLCPAQLP CEGSSEHRGG
     ERHLEPEESG PAKAEQEVQP GAVPFVALGG CPTGSSSLGV SIKPSLPGPG LTNNLQEELP
     STPAPQPTDT AGHQAGLSSV PTMHQGPEPH TQSPLLETVA TSSKGACAKE PIIEDSLPAS
     RSCDPGLIDS LKNYLLLLLK LSSTESGEAV TESPVGAATV GTALSPPLVP TVEVAGLSPR
     TSRRILERVE NNHLVQSAET LLLSPCTSRR LTSLLDQEVQ AGRQALASAQ AARGPGPSPL
     SVPAIVVGEE VPGVASEGSL EGPGLQSGQV AETKAHKPCQ EEREPGEALP GLPAATPEEL
     ALGARRKRFV PKVRAAGDGE VAKSEERESP SVSPRGPRKN LAPGSPGTPG RERRSPTQGK
     KAMLEVPRAE EEPVAGELGS SPKAGGPDAE PALDEDTQDP VAKTQKAKDL LKAPQVIRKI
     RVEQFPDASG SLKLWCQFFN ILNDSVLTWA KDQHPVGEVN RSAGDEGPAA LAIVQASPVD
     CGVYRCTIHN EHGSASTDFC LSPEVLSGFI SREEGEVGEE IEMTPMVFAK GLADSGCWGD
     KLFGRLVSEE LRGGGHGGGL QKASRAKVIY GLEPIFESGR TCIIKVSSLL VFGPSSETSL
     LGRNYDVTIQ GCKIQNMSRE YCKIFAAEAR AAPSFGEVPE IVPLYLIYRP ANTIPYATLE
     EDLGKSLQSY CSREGGCTGA PAAPSSSEIV QKCQAFQHWL YQWTNGSFLV TDLAGVDWKM
     TDVRIATKLR GYQGLKESCF PALLNHFASS HQCNAYCEML GLTALKGPEA SHPQAKPKVS
     KSPSAGRKGT QLSPQPQKKG PPSPQGTRRS TPSPKATSQA SEAAAVPGLG QPPSQEGGSK
     AHR
//
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